Abstract

In the normal processing of boPrPC, the protein is cleaved at two sites, between residues 121 and 122 in the amino acid sequence (N-terminal C1 cleavage site) and at the extreme C-terminal end (C-terminal cleavage site). However the abnormal form, PrPSc, seems to have an intact C1 cleavage site and is cleaved at an alternative site situated N-terminal to this site. Defining the mechanisms behind the formation of PrPSc from PrPC has become one of the central issues in understanding the pathogenesis of prion diseases. Knowledge about the factors governing the cleavages of PrP is an important issue in this part, since the cleavage is likely to be meaningful for the biological and pathological properties of the protein. We affected the cleavage of the bovine PrP by mutagenesis and inhibitor use and analysed what impact these treatments have on boPrP cell surface shedding and conformation. Furthermore, an analysis of the distribution of the different shedded PrP-fragments in the exosomal fraction and free in media was done

Published in

Conference

"Growth and Death in the Nervous System", Swiss Society of neuropathology, XXIst International Winter Meeting,

SLU Authors

• Klingeborn, Mikael

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

• Wik, Lotta

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

• Willander, Hanna

  • Department of Animal Biosciences, Swedish University of Agricultural Sciences
    

• Linne, Tommy

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Animal and Dairy Science
Veterinary Science


Permanent link to this page (URI)

https://res.slu.se/id/publ/22702